title: 31P-NMR investigation of trimethylphosphine binding to [alpha Fe(II), beta Mn(II)] hybrid hemoglobin. A model for partially liganded species.
abstract: 31P-NMR of trimethylphosphine binding to the ferrous chains of a ([alpha Fe(II), beta Mn(II)]hemoglobin hybrid is employed to investigate partially liganded species. This study shows that at low pH (6.5), in the presence of inositol hexaphosphate, the resonance at 23.2 ppm (from H3PO4) is due to phosphine bonding to alpha-chains in the T quaternary state. At elevated pH (7.6), phosphine binding to the alpha-chains produces a resonance at 24.8 ppm which is associated with a T-to-R conversion. These findings are discussed in relation with our previous results on direct observation of intermediate ligation states of hemoglobin.
authors.affiliation: Laboratoire de Chimie des Organométalliques, UA CNRS 415, Université de Rennes 1, France.
authors.forename: A
authors.initials: A
authors.lastname: Bondon
authors.forename: G
authors.initials: G
authors.lastname: Simonneaux
mesh_terms: D006441:Hemoglobin A / Q000378:metabolism*; D006801:Humans; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008345:Manganese / Q000378:metabolism; D010720:Phosphines / Q000378:metabolism*; D010758:Phosphorus; D011485:Protein Binding; D055503:Protein Multimerization
chemical_list: D008024:Ligands; D010720:Phosphines; D010758:Phosphorus; D008345:Manganese; C049750:trimethyl phosphine; D006441:Hemoglobin A